{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,19]],"date-time":"2026-09-19T20:05:37Z","timestamp":1789848337367,"version":"4.0.1"},"reference-count":69,"publisher":"Microbiology Society","issue":"5","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2005,5,1]]},"abstract":"<jats:p><jats:italic>Cryptococcus neoformans<\/jats:italic>is an important human fungal pathogen that also serves as a model for studies of fungal pathogenesis.<jats:italic>C. neoformans<\/jats:italic>contains several genes encoding peptidyl-prolyl<jats:italic>cis<\/jats:italic>\/<jats:italic>trans<\/jats:italic>isomerases (PPIases), enzymes that catalyse changes in the folding and conformation of target proteins. Three distinct classes of PPIases have been identified: cyclophilins, FK506-binding proteins (FKBPs) and parvulins. This paper reports the cloning and characterization of<jats:italic>ESS1<\/jats:italic>, which is believed to be the first (and probably only) parvulin-class PPIase in<jats:italic>C. neoformans<\/jats:italic>. It is shown that<jats:italic>ESS1<\/jats:italic>from<jats:italic>C. neoformans<\/jats:italic>is structurally and functionally homologous to<jats:italic>ESS1<\/jats:italic>from<jats:italic>Saccharomyces cerevisiae<\/jats:italic>, which encodes an essential PPIase that interacts with RNA polymerase II and plays a role in transcription. In<jats:italic>C. neoformans<\/jats:italic>,<jats:italic>ESS1<\/jats:italic>was found to be dispensable for growth, haploid fruiting and capsule formation. However,<jats:italic>ESS1<\/jats:italic>was required for virulence in a murine model of cryptococcosis. Loss of virulence might have been due to the defects in melanin and urease production observed in<jats:italic>ess1<\/jats:italic>mutants, or to defects in transcription of as-yet-unidentified virulence genes. The fact that Ess1 is not essential in<jats:italic>C. neoformans<\/jats:italic>suggests that, in this organism, some of its functions might be subsumed by other prolyl isomerases, in particular, cyclophilins Cpa1 or Cpa2. This is supported by the finding that<jats:italic>ess1<\/jats:italic>mutants were hypersensitive to cyclosporin A.<jats:italic>C. neoformans<\/jats:italic>might therefore be a useful organism in which to investigate crosstalk among different families of prolyl isomerases.<\/jats:p>","DOI":"10.1099\/mic.0.27786-0","type":"journal-article","created":{"date-parts":[[2005,5,3]],"date-time":"2005-05-03T21:28:21Z","timestamp":1115155701000},"page":"1593-1605","source":"Crossref","is-referenced-by-count":19,"title":["The Ess1 prolyl isomerase is dispensable for growth but required for virulence in Cryptococcus neoformans"],"prefix":"10.1099","volume":"151","author":[{"given":"Ping","family":"Ren","sequence":"first","affiliation":[{"name":"Mycology Laboratory, Wadsworth Center, New York State Department of Health, State University of New York, Albany, NY 12208, USA"},{"name":"Molecular Genetics Program, Wadsworth Center, New York State Department of Health, State University of New York, 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